ID N1WMF5_9LEPT Unreviewed; 790 AA.
AC N1WMF5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LEP1GSC060_3310 {ECO:0000313|EMBL:EMY76958.1};
OS Leptospira weilii serovar Ranarum str. ICFT.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1218598 {ECO:0000313|EMBL:EMY76958.1, ECO:0000313|Proteomes:UP000012313};
RN [1] {ECO:0000313|EMBL:EMY76958.1, ECO:0000313|Proteomes:UP000012313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICFT {ECO:0000313|EMBL:EMY76958.1,
RC ECO:0000313|Proteomes:UP000012313};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMY76958.1}.
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DR EMBL; AOHC02000041; EMY76958.1; -; Genomic_DNA.
DR AlphaFoldDB; N1WMF5; -.
DR STRING; 1218598.LEP1GSC060_3310; -.
DR Proteomes; UP000012313; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 153..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 411..632
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 663..780
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 712
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 790 AA; 91457 MW; DB8F7E9EFBED68F6 CRC64;
MQKSVYFRSF VYYFSDSENE NFQERIFAKD PSLSFRNIPA EMFSLGFTKT TAWFYIPLKN
DTEKEYYGIF EIYNPYLEEV DIHYRYGNQD RIQKISAGTN RVYEENFPTF DFYLRPGEEI
QIVCRIKSET PLRIPFVLES EKKYGFTKQL RSILVGLTIG FGIAMGLYNL SLYFFFREKS
YLYYFIMILF STAYLTSWDG LTLPLFKPEY GRYYLSVVLI LIYTSALFLF LFSFEFLYPE
KKEKKVQIVA IGYVVFSFLL MSLSIFYPTS LNRFSYYLGL INNLIIAYFC IVRIRDGFKS
AKNFLLIHMV FPIAGILTNL SAVEAISINY LSLHLLELAF ISQSVLFSIM LVQRIKELEY
KLKDGLQSEI HKNIILLKKE IQQRRETEWE LIQAKEVAEK AAKVKSSFLA NMSHEIRTPM
NGVLGMVQLL GTTKLNEEQK EYVNILSISA KSLLQIINDI LDFSKIEAGK ISLDKEVFSV
RSVLDEIHDL LYPLAKQKQI DFRLEGKFEI QEYVYGDQLR LRQILWNLTG NGIKFTNRGE
VVLNAFQKNI SKDKVSIEFT VLDSGIGIPF EKQKQVFDAF SQSDTSIARK FGGSGLGLSI
TKQLVELQGG VLSLESKEGR GSKFAFAITY DIPSESEIEK ILEAEKTKDL ESSYSNAVPK
SIKILVAEDN ETNRLLIERA LKKLGYDPFV VHNGREVIER MQLEFFDLIL MDIHMPEVDG
IEATRWIRSR KENAEFPIII ALTADAIDNS KEQYLVKGMN DCLFKPLDLP AFKKTLDFWS
DRVEASRRKL
//
